FEBS Letters | |
PDGF‐induced Akt phosphorylation does not activate NF‐κB in human vascular smooth muscle cells and fibroblasts | |
Rauch, Bernhard H.1  Weber, Artur-Aron1  Schrör, Karsten1  Zimmermann, Norbert2  Braun, Marina1  | |
[1] Institut für Pharmakologie und Klinische Pharmakologie, Heinrich-Heine-Universität Düsseldorf, Moorenstr. 5, 40225 Düsseldorf, Germany;Klinik für Thorax- und Kardiovaskuläre Chirurgie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany | |
关键词: Nuclear factor-κB; Akt phosphorylation; Cytokine; Growth factor; Vascular smooth muscle cell; EDTA; ethylenediamine-tetraacetic acid; IκB; inhibitory protein κB; NF-κB; nuclear factor κB; PBS; phosphate-buffered saline; PDGF; platelet-derived growth factor; SDS; sodium dodecyl sulfate; SMC; smooth muscle cells; TNFα; tumor necrosis factor-α; | |
DOI : 10.1016/S0014-5793(00)01957-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
A recent report suggested that platelet-derived growth factor (PDGF) activates nuclear factor-κB (NF-κB) by phosphorylation of the protein kinase Akt [Romashkova and Makarov, Nature 401 (1999) 86–90]. The present study investigates the role of Akt in the activation of NF-κB by tumor necrosis factor-α (TNFα, 10 ng/ml) and PDGF-BB (20 ng/ml) in human vascular smooth muscle cells (SMC), skin and foreskin fibroblasts. TNFα stimulated serine phosphorylation and degradation of the inhibitory protein IκBα and strongly induced nuclear NF-κB translocation and binding activity. PDGF did not induce serine phosphorylation or degradation of IκBα and did not enhance binding activity of NF-κB. In contrast, stimulation with PDGF resulted in a marked phosphorylation of Akt, but no Akt phosphorylation occurred after stimulation with TNFα. These data suggest that Akt phosphorylation is not involved in NF-κB activation in human SMC and fibroblasts.
【 授权许可】
Unknown
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